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| * '''Description:''' transcriptional regulator Spx, involved in regulation of many genes, important for the prevention of protein aggregation during severe heat stress, required for protection against paraquat stress <br/><br/>
| | {{#bank: Spx}} |
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| |style="background:#ABCDEF;" align="center"|'''Gene name'''
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| |''spx''
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| |style="background:#ABCDEF;" align="center"| '''Synonyms''' || ''yjbD ''
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| |style="background:#ABCDEF;" align="center"| '''Essential''' || no
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| |style="background:#ABCDEF;" align="center"| '''Product''' || transcriptional regulator Spx
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| |style="background:#ABCDEF;" align="center"|'''Function''' || negative and positive regulator of many genes
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| |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU11500 spx]
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| |colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://subtiwiki.uni-goettingen.de/interact/ ''Subt''Interact]''': [http://subtiwiki.uni-goettingen.de/interact/index.php?protein=Spx Spx]
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| |colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/subtipathways/search.php?enzyme=spx spx]'''
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| |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 15,5 kDa, 7.80
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| |style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 393 bp, 131 amino acids
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| |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[yjbC]]'', ''[[yjbE]]''
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| |style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU11500 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU11500 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU11500 DNA_with_flanks]
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| |colspan="2" | '''Genetic context''' <br/> [[Image:spx_context.gif]]
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| <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
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| |colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=spxA_1227697_1228092_1 Expression at a glance]'''   {{PubMed|22383849}}<br/>[[Image:spx_expression.png|500px|link=http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU11500]]
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| |}
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| __TOC__
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| <br/><br/><br/><br/>
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| <br/><br/><br/><br/>
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| <br/><br/><br/><br/>
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| <br/><br/>
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| = [[Categories]] containing this gene/protein =
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| {{SubtiWiki category|[[transcription factors and their control]]}},
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| {{SubtiWiki category|[[general stress proteins (controlled by SigB)]]}},
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| {{SubtiWiki category|[[cell envelope stress proteins (controlled by SigM, V, W, X, Y)]]}},
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| {{SubtiWiki category|[[resistance against oxidative and electrophile stress]]}},
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|
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| = This gene is a member of the following [[regulons]] =
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| {{SubtiWiki regulon|[[PerR regulon]]}},
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| {{SubtiWiki regulon|[[SigB regulon]]}},
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| {{SubtiWiki regulon|[[SigM regulon]]}},
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| {{SubtiWiki regulon|[[SigW regulon]]}},
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| {{SubtiWiki regulon|[[SigX regulon]]}}
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|
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| =The [[Spx regulon]]=
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| =The gene=
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| === Basic information ===
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| * '''Locus tag:''' BSU11500
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| ===Phenotypes of a mutant ===
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| * Loss of up-regulation of the methionine sulfoxide reductase (''[[msrA]]-[[msrB]]'') operon in response to thiol specific oxidative stress, also loss of ''[[trxA]]'' and ''[[trxB]]'' upregulation in response to thiol specific oxidative stress.
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| === Database entries ===
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| * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU11500&redirect=T BSU11500]
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| * '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/yjbCD.html]
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| * '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG13133 link]
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| === Additional information===
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| =The protein=
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| === Basic information/ Evolution ===
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| * '''Catalyzed reaction/ biological activity:'''
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| ** transcriptional regulator of many genes in response to thiol specific oxidative stress (transcription activator of'' [[trxA]]'' and ''[[trxB]]'')
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| ** in addition, Spx inhibits transcription by binding to the C-terminal domain of the alpha subunit of RNAP ([[RpoA]]), disrupting complex formation between RNAP and certain transcriptional activator proteins like [[ResD]] and [[ComA]]
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| ** in response to thiol specific oxidative stress, Spx can also activate transcription, making it a general regulator that exerts both positive and negative control over transcription initiation
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| ** involved in competence regulation {{PubMed|11703662}}
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| * '''Protein family:''' Spx subfamily (according to Swiss-Prot) Arsenate Reductase (ArsC) family, Spx subfamily
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| * '''Paralogous protein(s):''' [[MgsR]]
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|
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| === Extended information on the protein ===
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| * '''Kinetic information:'''
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| * '''[[Domains]]:''' CXXC (10-13): Acts as a disulfide switch for the redox-sensitive transcriptional regulation of genes that function in thiol homeostasis.
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| * '''Modification:''' Cysteine oxidation of the CXXC motif
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| * '''[[Cofactors]]:'''
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| * '''Effectors of protein activity:'''
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| * '''[[SubtInteract|Interactions]]:'''
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| ** [[Spx]]-[[YjbH]] [http://www.ncbi.nlm.nih.gov/sites/entrez/19074380 PubMed]
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| ** [[Spx]]-[[RpoA]] (C-terminal domain) {{PubMed|12642660,22307755}}
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| ** [[Spx]]-[[ClpP]]/[[ClpX]] (degradation of [[Spx]]) {{PubMed|17827297}}
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| * '''[[Localization]]:''' cytoplasm (according to Swiss-Prot)
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|
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| === Database entries ===
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| * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU11500&redirect=T BSU11500]
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| * '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=1Z3E 1Z3E] complex with C-terminal domain of [[RpoA]] [http://www.ncbi.nlm.nih.gov/Structure/mmdb/mmdbsrv.cgi?Dopt=s&uid=35536 NCBI]
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| * '''UniProt:''' [http://www.uniprot.org/uniprot/O31602 O31602]
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| * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU11500]
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| * '''E.C. number:'''
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| === Additional information===
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| =Expression and regulation=
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| * '''Operon:'''
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| ** ''[[yjbC]]-[[spx]]'' {{PubMed|10913081}}
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| ** ''[[spx]]'' {{PubMed|10913081}}
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| * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=spxA_1227697_1228092_1 spx] {{PubMed|22383849}}
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| * '''[[Sigma factor]]:'''
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| ** four promoters upstream of ''[[yjbC]]'': [[SigW]], [[SigB]], [[SigX]] [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+10913081 PubMed], [[SigM]] [http://www.ncbi.nlm.nih.gov/sites/entrez/17434969 PubMed]
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| ** promoters upstream of ''spx'': [[SigA]], [[SigW]] [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+10913081 PubMed], [[SigM]] [http://www.ncbi.nlm.nih.gov/sites/entrez/17434969 PubMed]
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| * '''Regulation:'''
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| ** induced by stress ([[SigB]]) [http://www.ncbi.nlm.nih.gov/pubmed/15805528 PubMed]
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| ** transcription is represed by [[PerR]] and [[YodB ]] [http://www.ncbi.nlm.nih.gov/sites/entrez/17158660 PubMed]
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| ** repressed in the absence of hydrogen peroxide ([[PerR]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/17158660 PubMed]
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| ** upregulated in response to enduracidin [http://www.ncbi.nlm.nih.gov/sites/entrez/20057163 PubMed]
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| * '''Regulatory mechanism:''' transcription repression
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| ** [[PerR]]: transcription repression [http://www.ncbi.nlm.nih.gov/sites/entrez/17158660 PubMed]
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| * '''Additional information:'''
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| ** post-translational control by [[ClpX]]-[[ClpP]]: Spx naturally contains a C-terminal sequence that resembles the [[SsrA]] tag and targets the protein for degradation. [http://www.ncbi.nlm.nih.gov/pubmed/12642660?ordinalpos=27&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DefaultReportPanel.Pubmed_RVDocSum PubMed]
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| ** proteolysis is enhanced by [[YjbH]] [http://www.ncbi.nlm.nih.gov/pubmed/19074380?ordinalpos=1&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DefaultReportPanel.Pubmed_RVDocSum PubMed] and counter-acted by [[YirB]] {{PubMed|21378193}}
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| ** the mRNA is substantially stabilized upon depletion of [[Rny|RNase Y]] (the half-life of the monocistronic ''spx'' mRNA increases from 1 to 6 min) {{PubMed|21815947}}
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| =Biological materials =
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| * '''Mutant:''' ORB6781 (spc), ORB6876 (tet), available in [[Zuber]] lab, also available in the [[Stülke]] lab
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| ** 1A917 ( ''spx''::''spec''), {{PubMed|21949854}}, available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1A917&Search=1A917 BGSC]
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| ** 1A916 ( ''spx''::''tet''), {{PubMed|21949854}}, available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1A916&Search=1A916 BGSC]
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| * '''Expression vector:'''
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| * '''lacZ fusion:'''
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| * '''GFP fusion:'''
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| * '''two-hybrid system:''' ''B. pertussis'' adenylate cyclase-based bacterial two hybrid system ([[BACTH]]), available in [[Stülke]] lab
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| * '''Antibody:'''
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| =Labs working on this gene/protein=
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| [[Peter Zuber]], Oregon Health and Science University, USA
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| [http://www.ogi.edu/people/dsp_person.cfm?person_id=411D6801-2A56-D16D-58A06B4480EDB9C7 Homepage]
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| [[Richard Brennan]], Houston, Texas, USA [http://www.mdanderson.org/departments/biochem/display.cfm?id=556ef368-6c81-4043-b74f350d41dd06cb&method=displayfull&pn=a8427ebd-d0ff-11d4-80fd00508b603a14 Homepage]
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| =Your additional remarks=
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| =References=
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| ==Reviews==
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| <pubmed> 19575568, 20626317</pubmed>
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| ==The [[Spx regulon]]==
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| <pubmed> 15937167, 14597697, 15028674, 22904090</pubmed>
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| ==Structural analysis of Spx==
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| <pubmed> 19580872, 16249335, 23813734 </pubmed>
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| ==Original Publications==
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| <pubmed>21378193,22307755 18487332,17908206,17434969,17158660, 19074380, 15805528, 18662407, 16885442, 18179421, 17434969, 17908206, 17158660, 11703662, 15659166, 12642660, 12057962, 10482513, 18687074, 12775685, 16740936, 17827297, 20084284 20057163 10913081 21815947 23894131 23934352 22582280 24417481 </pubmed>
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| [[Category:Protein-coding genes]]
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